Article

Distant site mutations in clinical TEM β-lactamase variants enhance non-covalent binding to ceftazidime: Insights from biophysical and in silico investigations

2025-10-01

Abstract excerpt

<title>Abstract</title> <p><bold>Purpose</bold>This study investigated the bioactive interactions of ceftazidime (CAZ) to TEM β-lactamase variants with distant site mutations isolated from clinical settings to explore the cause of their selection and dissemination due to empirical use of β-lactams.<bold>Methods</bold>Binding interactions of CAZ with wild-type and mutant (M184, M203, M210) TEM β-lactamases were re...

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Literature Corpus work: a14d5e69-e974-5b97-b3f4-73d951c6fbe5
DOI: 10.21203/rs.3.rs-7504842/v1

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Distant site mutations in clinical TEM β-lactamase variants enhance non-covalent binding to ceftazidime: Insights from biophysical and in silico investigationsDOI 10.21203/rs.3.rs-7504842/v1Read

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